Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.21.61 extracted from

  • Rockwell, N.C.; Krysan, D.J.; Fuller, R.S.
    Synthesis of Peptidyl Methylcoumarin Esters as Substrates and Active-Site Titrants for the Prohormone Processing Proteases Kex2 and PC2 (2000), Anal. Biochem., 280, 201-208.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.023
-
benzyloxycarbonyl-Ala-Tyr-Lys-Lys 4-methylcoumarin 7-amide pH 7.0, 21°C Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
yeast
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzyloxycarbonyl-Ala-Tyr-Lys-Lys 4-methylcoumarin 7-amide + H2O
-
Saccharomyces cerevisiae 7-amino-4-methylcoumarin + benzyloxycarbonyl-Ala-Tyr-Lys-Lys
-
?
benzyloxycarbonyl-Nle-Tyr-Lys-Lys 4-methylcoumarin 7-amide + H2O
-
Saccharomyces cerevisiae 7-amino-4-methylcoumarin + Cbz-Nle-Tyr-Lys-Lys
-
?

Synonyms

Synonyms Comment Organism
prohormone processing protease
-
Saccharomyces cerevisiae

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2640
-
benzyloxycarbonyl-Ala-Tyr-Lys-Lys 4-methylcoumarin 7-amide pH 7.0, 21°C Saccharomyces cerevisiae